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Sai Li

NameSai Li

Title: 副教授


E-mail sai (at) tsinghua.edu.cn

Address清华大学生物医学馆

Webhttp://www.lisailab.com


Education and professional experience:

2018-present  School of Life Sciences, Tsinghua University, China    Principal Investigator

2017-2018  Oxford Particle Imaging Centre, University of Oxford, UK       Senior Research Associate

2013-2017  Oxford Particle Imaging Centre, University of Oxford, UK    Postdoctoral Researcher

2009-2012  Physics department, University of Goettingen, Germany    Dr.rer.nat.

2006-2008  Physics department, University of Stuttgart, Germany    M.S.

2002-2006  School of Physics, Wuhan University, China    B.S.


Research Area:

My lab focuses on cryo-electron tomography (cryo-ET) and its application in in situ structural biology, especially in the assembly and disassembly of emerging enveloped viruses.

We aim at bridging dimensions between sub-nanometer resolution structures to micrometer scale in in situ landscapes, a soaring demand in the field of structural biology. To achieve this, we are active in developing cryo-ET methods, including: 1) cryo-ET and subtomogram averaging, 2) Focused-ion beam milling of cryo samples (FIB-SEM), and 3) Correlative light and electron microscopy (CLEM).

Among the many possible applications, we primarily study the assembly and disassembly of emerging enveloped viruses. Enveloped viruses, including the SARS-CoV-2, are the most threatening pathogens to the public health nowadays. Most enveloped viruses are very pleomorphic, cryo-ET and subtomogram averaging are the only way to provide high resolution information on their native structures. We aim to solve these questions: how are these viruses assembled and how do they disassemble, where are their weaknesses?


Selected Publications:

1. Sai Li: Cryo-electron tomography of enveloped viruses. Trends in Biochemical Sciences, 2021 (In press)

2. Joel D. Allen, Himanshi Chawla, Firdaus Samsudin, Lorena Zuzic, Aishwary Tukaram Shivgan, Yasunori Watanabe, Wan-ting He, Sean Callaghan, Ge Song, Peter Yong, Philip J. M. Brouwer, Yutong Song, Yongfei Cai, Helen M. E. Duyvesteyn, Tomas Malinauskas, Joeri Kint, Paco Pino, Maria J. Wurm, Martin Frank, Bing Chen, David I. Stuart, Rogier W. Sanders, Raiees Andrabi, Dennis R. Burton, Sai Li, Peter J. Bond, and Max Crispin: Site-Specific Steric Control of SARS-CoV 2 Spike Glycosylation. Biochemistry, 07/2021; DOI: 10.1021/acs.biochem.1c00279

1. Hangping Yao*, Yutong Song*, Yong Chen*, Nanping Wu*, Jialu Xu*, Chujie Sun, Jiaxing Zhang, Tianhao Weng, Zheyuan Zhang, Zhigang Wu, Linfang Cheng, Danrong Shi, Xiangyun Lu, Jianlin Lei, Max Crispin, Yigong Shi, Lanjuan Li#, and Sai Li#: Molecular architecture of the SARS-CoV-2 virus. Cell, 2020; DOI:10.1016/J.CELL.2020.09.018

2. Alexandra Serris, Robert Stass, Eduardo A. Bignon, Nicolas A. Muena, Jean-Claude Manuguerra, Rohit K. Jangra, Sai Li, Kartik Chandran, Nicole Tischler, Juha T. Huiskonen, Felix A. Rey, and Pablo Guardado-Calvo: Description of the Hantavirus Surface Glycoprotein Lattice and Its Membrane Fusion Control Mechanism. Cell, 2020; DOI:10.1016/J.CELL.2020.08.023

3. Ying Liu*, Yutong Song*, Siyu Zhang, Min Diao, Shanjin Huang, Sai Li, and Xu Tan: PSGL-1 inhibits HIV-1 infection by restricting actin dynamics and sequestering HIV envelope proteins. Cell Discovery, 12/2020; DOI:10.1038/s41421-020-0184-9

4. Yanqing Zhang*, Sai Li*, Xuechen Zhu*, Gaoxingyu Huang*, Chao Zeng*, Qifan Wang, Kunpeng Wang, Qiang Zhou, Wusheng Zhang, Guangwen Yang, Minhao Liu, Qinghua Tao, Jianlin Lei, and Yigong Shi: Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex. Cell Research, 05/2020; DOI:10.1038/s41422-020-0320-y

5. Xiaoling Wu*, Hua Yue*, Yuanyu Zhang*, Xiaoyong Gao, Xiaoyang Li, Licheng Wang, Yufei Cao, Miao Hou, Haixia An, Lin Zhang#, Sai Li#, Jingyuan Ma, He Lin, Yanan Fu, Hongkai Gu, Wenyong Lou, Wei Wei#, Richard N. Zare, and Jun Ge#: Packaging and delivering enzymes by amorphous metal-organic frameworks. Nature Communications, 11/2019; 10(1)., DOI:10.1038/s41467-019-13153-x

6. Kamel El Omari, Sai Li, Abhay Kotecha, Thomas S Walter, Eduardo Andres Bignon, Karl Harlos, Pentti Somerharju, Felix De Haas, Daniel K. Clare, Mika Molin, Felipe Hurtado, Mengqiu Li, Jonathan M. Grimes, Dennis H. Bamford, Nicole D. Tischler, Juha T. Huiskonen, David I. Stuart, Elina Roine: The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins. Nature Communications, 02/2019; 10(1)., DOI:10.1038/s41467-019-08728-7

7. Steinar Halldorsson*, Sai Li*, Mengqiu Li, Karl Harlos, Thomas A. Bowden, Juha T. Huiskonen: Shielding and activation of a viral membrane fusion protein. Nature Communications, 01/2018; 9(349)., DOI:10.1038/s41467-017-02789-2

8. Sai Li, Ilona Rissanen, Antra Zeltina, Jussi Hepojoki, Jayna Raghwani, Karl Harlos, Oliver G. Pybus, Juha T. Huiskonen, Thomas A. Bowden: A Molecular-Level Account of the Antigenic Hantaviral Surface. Cell Reports, 06/2016; 16(1):278., DOI:10.1016/j.celrep.2016.06.039

9. Sai Li, Zhaoyang Sun, Rhys Pryce, Marie-Laure Parsy, Sarah K Fehling, Katrin Schlie, C Alistair Siebert, Wolfgang Garten, Thomas A Bowden, Thomas Strecker, Juha T Huiskonen: Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike. PLoS Pathogens, 02/2016; 12(2)., DOI:10.1371/journal.ppat.1005418

10. Sai Li*, Christian Sieben*, Kai Ludwig, Chris T Höfer, Salvatore Chiantia, Andreas Herrmann, Frederic Eghiaian, Iwan A.T. Schaap: pH-Controlled Two-Step Uncoating of Influenza Virus. Biophysical Journal, 04/2014; 106(7):1447-56., DOI:10.1016/j.bpj.2014.02.018

11. Sai Li, Frederic Eghiaian, Christian Sieben, Andreas Herrmann, Iwan A.T. Schaap: Bending and Puncturing the Influenza Lipid Envelope. Biophysical Journal, 02/2011; 100(3):637-45., DOI:10.1016/j.bpj.2010.12.3701

12. Felix Hoos, Sai Li, Todd Meyrath, Bernd Braun, and Harald Giessen: Thermal lensing in an end-pumped Yb:KGW slab laser with high power single emitter diodes. Optics Express, 04/2008; 16(9):6041-9., DOI:10.1364/OE.16.006041

# Corresponding Author; * Equal contribution


 

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